Projects per year
Abstract
"Cohort-ry" in motion: The chemistry following Co-C bond homolysis in coenzyme B 12-dependent ethanolamine ammonia lyase is known to favor dissociation, but what of the protein contribution? Experiments reveal the radical pair reaction dynamics to be coupled to the ps-ns protein dynamics in B 12 photolysis. This raises the possibility of a subtle, dynamic contribution to homolysis, which acts in cohort with electrostatics and H-abstraction from the substrate. © 2011 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original language | English |
---|---|
Pages (from-to) | 10843-10846 |
Number of pages | 3 |
Journal | Angewandte Chemie - International Edition |
Volume | 50 |
Issue number | 46 |
DOIs | |
Publication status | Published - 11 Nov 2011 |
Keywords
- coenzyme B 12
- enzyme catalysis
- magnetic field effects
- protein dynamics
- radical pair reactions
Research Beacons, Institutes and Platforms
- Photon Science Institute
Fingerprint
Dive into the research topics of 'Is there a dynamic protein contribution to the substrate trigger in coenzyme B 12-dependent ethanolamine ammonia lyase?'. Together they form a unique fingerprint.Projects
- 1 Finished
-
Linking experiment to theory: Quantum entanglement during enzyme catalysis - Dr S Hay fellowship
Hay, S. (PI)
1/09/10 → 31/08/15
Project: Research